Journal
JOURNAL OF CELL BIOLOGY
Volume 183, Issue 7, Pages 1223-1233Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200809190
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Funding
- Deutsche Forschungsgemeinschaft
- European Union
- Swiss National Science Foundation ( SNSF)
- Centre National de la Recherche Scientifique
- Association de la Recherche contre le Cancer [3140]
- French National Research Agency ( ANR) [JC05_42022]
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The microtubule cytoskeleton is crucial for the internal organization of eukaryotic cells. Several microtubule-associated proteins link microtubules to subcellular structures. A subclass of these proteins, the plus end-binding proteins (+TIPs), selectively binds to the growing plus ends of microtubules. Here, we reconstitute a vertebrate plus end tracking system composed of the most prominent +TIPs, end-binding protein 1 (EB1) and CLIP-170, in vitro and dissect their end-tracking mechanism. We. find that EB1 autonomously recognizes specific binding sites present at growing microtubule ends. In contrast, CLIP-170 does not end-track by itself but requires EB1. CLIP-170 recognizes and turns over rapidly on composite binding sites constituted by end-accumulated EB1 and tyrosinated alpha-tubulin. In contrast to its. fission yeast orthologue Tip1, dynamic end tracking of CLIP-170 does not require the activity of a molecular motor. Our results demonstrate evolutionary diversity of the plus end recognition mechanism of CLIP-170 family members, whereas the autonomous end-tracking mechanism of EB family members is conserved.
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